Ontology highlight
ABSTRACT:
SUBMITTER: Guo J
PROVIDER: S-EPMC4286514 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20141224 1
Allostery is an essential means for regulating biomolecular functions and provides unique opportunities for drug design, yet our ability to elucidate allosteric mechanisms remains limited. Here, based on extensive molecular dynamics simulations, we present an atomistic picture of the pathways mediating the allosteric regulation of the PPIase domain of Pin1 by its WW domain. Two pathways jointly propagate the action of substrate-WW binding to produce closure and rigidification of three PPIase cat ...[more]